Dong_2020_Bioresour.Bioprocess_7_37

Reference

Title : Structure-guided engineering of a Thermobifida fusca cutinase for enhanced hydrolysis on natural polyester substrate - Dong_2020_Bioresour.Bioprocess_7_37
Author(s) : Dong Q , Yuan S , Wu L , Su L , Zhao Q , Wu J , Huang W , Zhou J
Ref : Bioresour. Bioprocess , 7 :37 , 2020
Abstract : Cutinases could degrade insoluble polyester, including natural cutin and synthetic plastic. However, their turnover efficiency for polyester remains too low for industrial application. Herein, we report the 1.54-A resolution X-ray crystal structure of a cutinase from Thermobifida fusca and modeling structure in complex with a cutin mimic oligo-polyester C24H42O8. These efforts subsequently guided our design of cutinase variants with less bulky residues in the vicinity of the substrate binding site. The L90A and I213A variants exhibit increased hydrolysis activity (5- and 2.4-fold, respectively) toward cutin and also showed enhanced cotton scouring efficiency compared with the wild-type enzyme.
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Gene_locus related to this paper: thefu-q6a0i4

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Gene_locus related to this paper: thefu-q6a0i4

Citations formats

Dong Q, Yuan S, Wu L, Su L, Zhao Q, Wu J, Huang W, Zhou J (2020)
Structure-guided engineering of a Thermobifida fusca cutinase for enhanced hydrolysis on natural polyester substrate
Bioresour. Bioprocess 7 :37

Dong Q, Yuan S, Wu L, Su L, Zhao Q, Wu J, Huang W, Zhou J (2020)
Bioresour. Bioprocess 7 :37